Crystal structure of the read‐through domain from bacteriophage Qβ A1 protein

Bacteriophage Qβ is a small RNA virus that infects Escherichia coli. The virus particle contains a few copies of the minor coat protein A1, a C‐terminally prolonged version of the coat protein, which is formed when ribosomes occasionally read‐through the leaky stop codon of the coat protein. The cry...

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Vydané v:Protein science Ročník 20; číslo 10; s. 1707 - 1712
Hlavní autori: Rumnieks, Janis, Tars, Kaspars
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: Hoboken Wiley Subscription Services, Inc., A Wiley Company 01.10.2011
Predmet:
allolevivirus
Allolevivirus - chemistry
Amino Acid Sequence
bacteriophage Qβ
Capsid Proteins - chemistry
Crystallography, X-Ray
Escherichia coli
Leviviridae
minor coat protein
Models, Molecular
Molecular Sequence Data
polyproline helix
Protein Structure, Secondary
Protein Structure, Tertiary
read‐through protein
Sequence Alignment
small RNA phages
ISSN:0961-8368, 1469-896X, 1469-896X
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Popis
Shrnutí:Bacteriophage Qβ is a small RNA virus that infects Escherichia coli. The virus particle contains a few copies of the minor coat protein A1, a C‐terminally prolonged version of the coat protein, which is formed when ribosomes occasionally read‐through the leaky stop codon of the coat protein. The crystal structure of the read‐through domain from bacteriophage Qβ A1 protein was determined at a resolution of 1.8 Å. The domain consists of a heavily deformed five‐stranded β‐barrel on one side of the protein and a β‐hairpin and a three‐stranded β‐sheet on the other. Several short helices and well‐ordered loops are also present throughout the protein. The N‐terminal part of the read‐through domain contains a prominent polyproline type II helix. The overall fold of the domain is not similar to any published structure in the Protein Data Bank. PDB Code(s): 3RLC, 3RLK
Bibliografia:ObjectType-Article-1
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ObjectType-Feature-2
content type line 23
Additional Supporting Information may be found in the online version of this article.
Grant sponsor: European Social Fund; Grant number: 1DP/1.1.1.2.0/09/APIA/VIAA/150; Grant sponsor: Latvian Council of Science; Grant number: 09.1294; Grant sponsor: European Social Fund (Support for Doctoral Studies at University of Latvia); Grant number: 2009/0138/1DP/1.1.2.1.2/09/IPIA/VIAA/004 (J.R.).
ISSN:0961-8368
1469-896X
1469-896X
DOI:10.1002/pro.704